about
Dynamically Coupled Residues within the SH2 Domain of FYN Are Key to Unlocking Its ActivityFrom Binding-Induced Dynamic Effects in SH3 Structures to Evolutionary Conserved SectorsQuantifying information transfer by protein domains: analysis of the Fyn SH2 domain structureAccurate prediction of the dynamical changes within the second PDZ domain of PTP1e.Cooperation prevails when individuals adjust their social tiesReconstruction of protein backbones from the BriX collection of canonical protein fragmentsThe evolution of prompt reaction to adverse ties.Information theoretical quantification of cooperativity in signalling complexes.When agreement-accepting free-riders are a necessary evil for the evolution of cooperationEvolutionary dynamics of social dilemmas in structured heterogeneous populations.Stochastic simulation of the chemoton.Avoiding or restricting defectors in public goods games?Generosity motivated by acceptance--evolutionary analysis of an anticipation game.DEOGEN2: prediction and interactive visualization of single amino acid variant deleteriousness in human proteins.Dynamics of mutant cells in hierarchical organized tissues.Structural insights into the intertwined dimer of fyn SH2Multilevel biological characterization of exomic variants at the protein level significantly improves the identification of their deleterious effects.Tyrosine kinase inhibitor therapy can cure chronic myeloid leukemia without hitting leukemic stem cells.Good agreements make good friendsPurification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide.Synergy between intention recognition and commitments in cooperation dilemmas.Evolutionary dynamics of chronic myeloid leukemia.On the dynamics of neutral mutations in a mathematical model for a homogeneous stem cell population.The DynaMine webserver: predicting protein dynamics from sequence.¹H, ¹³C and ¹⁵N backbone and side-chain chemical shift assignments of the free and bound forms of the human PTPN11 second SH2 domain.1H, 13C and 15N backbone and side-chain chemical shift assignment of the Fyn SH2 domain and its complex with a phosphotyrosine peptide.From protein sequence to dynamics and disorder with DynaMine.Protein domains as information processing units.Protein-peptide interactions adopt the same structural motifs as monomeric protein folds.Explaining the in vitro and in vivo differences in leukemia therapy.The evolutionary language game: an orthogonal approach.Chemical shift assignments of the partially deuterated Fyn SH2-SH3 domain.Equivalence of cooperation indexes: Comment on "Universal scaling for the dilemma strength in evolutionary games" by Z. Wang et al.Evolution of complexity.Special issue for the 20th Anniversary of the European Conference on Artificial Life (ECAL 2011).A synthon approach to artificial chemistry.Emergence of fairness in repeated group interactions.The role of diversity in the evolution of cooperation.Reacting differently to adverse ties promotes cooperation in social networks.Structural Characterization of Monomeric/Dimeric State of p59fyn SH2 Domain.
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P50
description
hulumtues
@sq
onderzoeker
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researcher
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հետազոտող
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name
Tom Lenaerts
@ast
Tom Lenaerts
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Tom Lenaerts
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Tom Lenaerts
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type
label
Tom Lenaerts
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Tom Lenaerts
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Tom Lenaerts
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Tom Lenaerts
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Tom Lenaerts
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Tom Lenaerts
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Tom Lenaerts
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Tom Lenaerts
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P108
P1053
B-6376-2008
P106
P1153
8643861100
P21
P2456
P2798
P31
P3829
P496
0000-0003-3645-1455